Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
about
Sequence co-evolutionary information is a natural partner to minimally-frustrated models of biomolecular dynamicsProkaryotic 2-component systems and the OmpR/PhoB superfamilyPhytochromes: an atomic perspective on photoactivation and signalingNegative control in two-component signal transduction by transmitter phosphatase activityCell fate regulation governed by a repurposed bacterial histidine kinaseIdentical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrateUsing Structural Information to Change the Phosphotransfer Specificity of a Two-Component Chemotaxis Signalling ComplexStructural Characterization of the Predominant Family of Histidine Kinase Sensor DomainsStructural and Enzymatic Insights into the ATP Binding and Autophosphorylation Mechanism of a Sensor Histidine KinaseRegulation of Response Regulator Autophosphorylation through Interdomain ContactsA structural model of anti-anti-σ inhibition by a two-component receiver domain: the PhyR stress response regulatorPeriplasmic domain of the sensor-kinase BvgS reveals a new paradigm for the Venus flytrap mechanismStructural Basis for Two-component System Inhibition and Pilus Sensing by the Auxiliary CpxP ProteinStructural insights into ChpT, an essential dimeric histidine phosphotransferase regulating the cell cycle inCaulobacter crescentusMechanistic Insights Revealed by the Crystal Structure of a Histidine Kinase with Signal Transducer and Sensor DomainsActivation of ATP Binding for the Autophosphorylation of DosS, a Mycobacterium tuberculosis Histidine Kinase Lacking an ATP Lid MotifSolution Structure of a Complex of the Histidine Autokinase CheA with Its Substrate CheYBranched Signal Wiring of an Essential Bacterial Cell-Cycle Phosphotransfer ProteinStructural Basis of a Rationally Rewired Protein-Protein Interface Critical to Bacterial SignalingSegmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylationDimerization properties of the RpBphP2 chromophore-binding domain crystallized by homologue-directed mutagenesisInfluence of the AgrC-AgrA Complex on the Response Time of Staphylococcus aureus Quorum SensingCrystal structures of apparent saccharide sensors from histidine kinase receptors prevalent in a human gut symbiontVisualizing autophosphorylation in histidine kinasesGeneral Stress Signaling in the AlphaproteobacteriaAncestral genes can control the ability of horizontally acquired loci to confer new traitsGenetic and biochemical dissection of a HisKA domain identifies residues required exclusively for kinase and phosphatase activitiesTwo-component regulatory systems in Pseudomonas aeruginosa: an intricate network mediating fimbrial and efflux pump gene expressionFlexible backbone sampling methods to model and design protein alternative conformationsThe regulatory factor SipA is a highly stable beta-II class protein with a SH3 fold.A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.Simultaneous identification of specifically interacting paralogs and interprotein contacts by direct coupling analysis.Probing designability via a generalized model of helical bundle geometryHigh-resolution protein complexes from integrating genomic information with molecular simulation.Overproduced Brucella abortus PdhS-mCherry forms soluble aggregates in Escherichia coli, partially associating with mobile foci of IbpA-YFP.The S helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12.Role of the VirA histidine autokinase of Agrobacterium tumefaciens in the initial steps of pathogenesisSystematic dissection and trajectory-scanning mutagenesis of the molecular interface that ensures specificity of two-component signaling pathways.Protein histidine kinases: assembly of active sites and their regulation in signaling pathways.Interaction fidelity in two-component signaling.
P2860
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P2860
Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
description
2009 nî lūn-bûn
@nan
2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Structural insight into partne ...... -component signal transduction
@ast
Structural insight into partne ...... -component signal transduction
@en
Structural insight into partne ...... -component signal transduction
@nl
type
label
Structural insight into partne ...... -component signal transduction
@ast
Structural insight into partne ...... -component signal transduction
@en
Structural insight into partne ...... -component signal transduction
@nl
prefLabel
Structural insight into partne ...... -component signal transduction
@ast
Structural insight into partne ...... -component signal transduction
@en
Structural insight into partne ...... -component signal transduction
@nl
P50
P3181
P1433
P1476
Structural insight into partne ...... -component signal transduction
@en
P2093
Alberto Marina
P304
P3181
P356
10.1016/J.CELL.2009.08.032
P407
P577
2009-10-01T00:00:00Z